The bile-salt-stimulated lipase in human milk. Purification and characterization.

The bile-salt-stimulated lipase was purified from human whey by chromatography on heparin-Sepharose and Affi-Gel blue. The purified enzyme gave a single band with a molecular weight of 90 000 on dodecylsulphate/polyacrylamide gels and this band accounted for at least 98% of the protein on the gel. An antiserum to the purified lipase completely inhibited the enzyme activity and gave a single precipitate against human whey and purified lipase. The bile-salt-stimulated lipase was inhibited by diisopropylfluorophosphate, which bound to the purified enzyme in a molar ratio of 0.85 mol/mol. The lipase is a glycoprotein with a high content of acidic amino acid residues and an isoelectric point of around 4. Proline constitutes more than 10% of the total amino acid residues. The purified lipase has a turnover number of around 150 S-1.